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Database: UniProt
Entry: R7YMW9_CONA1
LinkDB: R7YMW9_CONA1
Original site: R7YMW9_CONA1 
ID   R7YMW9_CONA1            Unreviewed;       785 AA.
AC   R7YMW9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   13-SEP-2023, entry version 43.
DE   RecName: Full=3-methylcrotonyl-CoA carboxylase alpha subunit {ECO:0008006|Google:ProtNLM};
GN   ORFNames=W97_02366 {ECO:0000313|EMBL:EON63139.1};
OS   Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Coniosporium.
OX   NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON63139.1, ECO:0000313|Proteomes:UP000016924};
RN   [1] {ECO:0000313|Proteomes:UP000016924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Coniosporium apollinis CBS 100218.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; JH767561; EON63139.1; -; Genomic_DNA.
DR   RefSeq; XP_007778456.1; XM_007780266.1.
DR   AlphaFoldDB; R7YMW9; -.
DR   STRING; 1168221.R7YMW9; -.
DR   GeneID; 19899677; -.
DR   eggNOG; KOG0238; Eukaryota.
DR   HOGENOM; CLU_000395_3_1_1; -.
DR   OMA; RDIRYET; -.
DR   OrthoDB; 1459320at2759; -.
DR   Proteomes; UP000016924; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000016924}.
FT   DOMAIN          22..483
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          143..343
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          714..785
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   785 AA;  86954 MW;  32D408BC503339BC CRC64;
     MAIEKLPQRI FDQIQDDAGR PLIKRLLIAN RGEIACRVVA TCRKLNITSI AVYTDPDTHS
     LHVQEADEAV RLGAIDGPEG NPHQNIQLLI QTALAHNADA IHPGYGYLSE NAEFSRQVRE
     AGIIFLGPSP NSMAILGDKR SAKQYLLKNA PKIPLIPGYN GTEQTVDRLL IEADRIGFPI
     LIKASAGGGG KGMRIVRHRE QLRDELNRAQ SEAQRSFGSS DCILERYIQR SKHIEIQILG
     DNHGTIVSLM DRECSIQRRH QKIIEEAPSP WLKPALRQKM SETAVAIGKL LDYESAGTVE
     FIVDVETTEF FFLEVNTRIQ VEHPITEETT GVDIVGLQIF VAGGGHLDDL GYWHDGMAPQ
     VGHAIECRLC AEDPSRDFMP DLGFLRQWKT ASEILPSAQT QDVRFETGIA TGSQVSIYFD
     SLIAKIVVWA PTRRQAIEKM VKMLAYTVCI GIRSNQSFLQ SCLLHPKFRD PEYSTSFIPD
     LLPTLIKNPY VDDLLATQGK LSFLPSILRR QASLPSVQNN RQSFRSLPRS FRNQKADLAN
     AQADVVLVPA HPEKIFIVAW PSSRSPEKFH NVTILPLSKQ DIQKSTEKVS SEDVKPSIQL
     ALDYNQVSSH VRQLPRPGQT SSLSHEVSLS IRATSVFQQT PDSTWHLHEL FVSVDTQRYT
     VFAVSAASSP GTDVGSHQKF FAHIPALGTY IEYNLCSLLT YGESLRKDTG ESAVASQRSP
     KAPMPCKVLN VAKKDGETVK VGEIAVVVES MKMEMNILAA AEGIFRAKVA MGEAVEEGTV
     LFTIS
//
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